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| | <StructureSection load='6n12' size='340' side='right'caption='[[6n12]], [[Resolution|resolution]] 2.23Å' scene=''> | | <StructureSection load='6n12' size='340' side='right'caption='[[6n12]], [[Resolution|resolution]] 2.23Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n12]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N12 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n12]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N12 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.23Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n0b|6n0b]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SEPT7, CDC10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6n12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n12 OCA], [https://pdbe.org/6n12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n12 RCSB], [https://www.ebi.ac.uk/pdbsum/6n12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n12 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6n12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n12 OCA], [http://pdbe.org/6n12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n12 RCSB], [http://www.ebi.ac.uk/pdbsum/6n12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n12 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SEPT7_HUMAN SEPT7_HUMAN]] Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.<ref>PMID:17803907</ref> <ref>PMID:18460473</ref> | + | [https://www.uniprot.org/uniprot/SEPT7_HUMAN SEPT7_HUMAN] Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.<ref>PMID:17803907</ref> <ref>PMID:18460473</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Araujo, A P.U]] | + | [[Category: Araujo APU]] |
| - | [[Category: Brandao-Neto, J]] | + | [[Category: Brandao-Neto J]] |
| - | [[Category: Brognara, G]] | + | [[Category: Brognara G]] |
| - | [[Category: Garratt, R C]] | + | [[Category: Garratt RC]] |
| - | [[Category: Pereira, H M]] | + | [[Category: Pereira HM]] |
| - | [[Category: Cytoskeleton component septin gtpase]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
SEPT7_HUMAN Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements.[1] [2]
Publication Abstract from PubMed
Septins are GTP-binding proteins that will often spontaneously assemble into filaments. In some species, particularly budding yeast, it is well known that these are capable of associating with membranes in order to fulfill their cellular role as a component of the cytoskeleton. Different from other human septins, SEPT7 appears to be unique in that it is an essential component of all hetero-oligomeric complexes described to date. As a step towards understanding the molecular basis of filament assembly, here we present two high-resolution structures of the SEPT7 GTPase domain complexed with GDP. One of these reveals a previously unreported coordination for the magnesium ion involving four water molecules and only a tenuous connection to the protein. The higher resolution structures provide unambiguous insight into the interactions at the G-interface where a structural motif based on an antiparallel beta-bridge allows for the rationalization of why some septins show nucleotide-dependent beta-strand slippage and others do not.
Revisiting SEPT7 and the slippage of beta-strands in the septin family.,Brognara G, Pereira HM, Brandao-Neto J, Araujo APU, Garratt RC J Struct Biol. 2019 Apr 19. pii: S1047-8477(19)30081-4. doi:, 10.1016/j.jsb.2019.04.015. PMID:31009756[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kremer BE, Adang LA, Macara IG. Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell. 2007 Sep 7;130(5):837-50. PMID:17803907 doi:http://dx.doi.org/10.1016/j.cell.2007.06.053
- ↑ Zhu M, Wang F, Yan F, Yao PY, Du J, Gao X, Wang X, Wu Q, Ward T, Li J, Kioko S, Hu R, Xie W, Ding X, Yao X. Septin 7 interacts with centromere-associated protein E and is required for its kinetochore localization. J Biol Chem. 2008 Jul 4;283(27):18916-25. doi: 10.1074/jbc.M710591200. Epub 2008 , May 6. PMID:18460473 doi:http://dx.doi.org/10.1074/jbc.M710591200
- ↑ Brognara G, Pereira HM, Brandao-Neto J, Araujo APU, Garratt RC. Revisiting SEPT7 and the slippage of beta-strands in the septin family. J Struct Biol. 2019 Apr 19. pii: S1047-8477(19)30081-4. doi:, 10.1016/j.jsb.2019.04.015. PMID:31009756 doi:http://dx.doi.org/10.1016/j.jsb.2019.04.015
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